Structure determination of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis.
Acta Crystallogr F Struct Biol Commun
; 70(Pt 2): 156-9, 2014 Feb.
Article
em En
| MEDLINE
| ID: mdl-24637747
ABSTRACT
Polysaccharide deacetylases are bacterial enzymes that catalyze the deacetylation of acetylated sugars on the membranes of Gram-positive bacteria, allowing them to be unrecognized by host immune systems. Inhibition of these enzymes would disrupt such pathogenic defensive mechanisms and therefore offers a promising route for the development of novel antibiotic therapeutics. Here, the first X-ray crystal structure of BA0150, a putative polysaccharide deacetylase from Bacillus anthracis, is reported to 2.0 Å resolution. The overall structure maintains the conserved (α/ß)8 fold that is characteristic of this family of enzymes. The lack of a catalytic metal ion and a distinctive metal-binding site, however, suggest that this enzyme is not a functional polysaccharide deacetylase.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bacillus anthracis
/
Amidoidrolases
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2014
Tipo de documento:
Article